Stability improvement of human collagen α1(I) chain using insulin as a fusion partner

Yu Mi; Yuan Gao; Daidi Fan; Zhiguang Duan; Rongzhan Fu; Lihua Liang; Wenjiao Xue; Shanshan Wang

doi:10.1016/j.cjche.2018.04.008

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Stability improvement of human collagen α1(I) chain using insulin as a fusion partner

Biotechnology and Bioengineering | Updated：2026-01-06

- Stability improvement of human collagen α1(I) chain using insulin as a fusion partner
- Chinese Journal of Chemical Engineering Vol. 26, Issue 12, Pages: 2607-2614(2018)
- Affiliations：
  
  1. 2 Shaanxi Institute of Microbiology,Xi'an,China,710043
  2. 3 School of Biological Science and Engineering, Shaanxi University of Technology,Hanzhong,China,723001
- Author bio：
- Funds：
- DOI：10.1016/j.cjche.2018.04.008
  CLC：
- Published：2018
- Accepted：
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Yu Mi, Yuan Gao, Daidi Fan, Zhiguang Duan, Rongzhan Fu, Lihua Liang, Wenjiao Xue, Shanshan Wang. Stability improvement of human collagen α1(I) chain using insulin as a fusion partner[J]. Chin.J.Chem.Eng., 2018, 26(12): 2607-2614.
DOI：

Yu Mi, Yuan Gao, Daidi Fan, Zhiguang Duan, Rongzhan Fu, Lihua Liang, Wenjiao Xue, Shanshan Wang. Stability improvement of human collagen α1(I) chain using insulin as a fusion partner[J]. Chin.J.Chem.Eng., 2018, 26(12): 2607-2614. DOI： 10.1016/j.cjche.2018.04.008.

摘要

Abstract

To enhance the stability of recombinant human collagen α1(I) chains (rhCOL1A1) in production and purification stages

a gene fragment fusing COL1A1 and insulin protein coding domains was synthesized and inserted into the pPIC9K expression vector. The fusion peptide-expressing Pichia pastoris strain was created by transformation. After optimization of shake flask cultures

the ultimate intracellular expression level of the insulin-collagen α1 (I) chain fusion protein (INS-COL1A1) reached about 300 mg·L

-1

and no obvious protein degradation was found in the fermentation and purification processes. The His-tagged recombinant fusion protein was detected by western blotting and was effectively purified using Ni

-chelating chromatography. A prominent improvement in the stability of INS-COL1A1 was observed compared to rhCOL1A1 in vitro

and the rhCOL1A1 released from the fusion protein was studied by LC-MS/MS and in bioassays. The results showed that the purified rhCOL1A1 was consistent with the native protein in amino acid composition and had a similar biological compatibility. To our knowledge

this is the first study to demonstrate the use of insulin as a fusion protein to improve the sta

bility of easily degradable proteins.

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